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Glucagon-like peptide 1 has a physiological role in the control of postprandial glucose in humans: studies with the antagonist exendin 9-39.
Abstract
Glucagon-like peptide 1(7-36) amide (GLP-1) is postulated to be the major physiological incretin in humans, but evidence is indirect. We report the first studies examining the physiological role of GLP-1 in the postprandial state in humans using the GLP-1 antagonist exendin 9-39. Exendin 9-39 completely blocked GLP-1-induced glucose-stimulated insulin release from perifused human islets of Langerhans. In healthy fasted volunteers, intravenous infusion of exendin 9-39 at 500 pmol x kg(-1) x min(-1) in the hyperglycemic state abolished the insulinotropic effect of a physiological dose of GLP-1 and fully reversed the glucose-lowering effect of GLP-1. Nine healthy subjects consumed a 150-g oral glucose tolerance test and were infused with 500 pmol x kg(-1) x min(-1) exendin 9-39 or saline. Exendin 9-39 increased the peak postprandial glucose level (exendin 9-39, 8.67 +/- 0.35 vs. saline, 7.67 +/- 0.35 mmol/l, P < or = 0.005) and increased postprandial plasma glucose incremental area under the curve by 35% (exendin 9-39, 152 +/- 19 vs. saline, 113 +/- 16 mmol x min x l(-1), P < or = 0.05). This could be explained as partly secondary to the blockade of glucose-induced suppression of glucagon and maybe also to an increased rate of gastric emptying. Thus, in humans exendin 9-39 acts as an antagonist of GLP-1 both in vitro and in vivo. When infused alone, exendin 9-39 causes a deterioration in postprandial glycemic control, suggesting that GLP-1 may be important for maintenance of normal postprandial glucose homeostasis in humans.
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“This peptide is known to impair oral glucose tolerance, resulting in a greater glucose AUC compared to saline (8).”
From Assessment of the incretin effect in healthy subjects: concordance between clamp and OGTT methods (2023) · cites this paper as [8]
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“A variety of studies using different and complementary methods to block the effects of the incretins have clearly demonstrated that GIP and GLP-1 are necessary for normal glucose homeostasis [5-16].”
BackgroundThe role of the gut hormone GLP-1 in the metabolic improvements caused by ileal transposition
Gaitonde, S. G., Kohli, R., & Seeley, R. J. (2011) · Journal of Surgical Research · doi:10.1016/j.jss.2011.04.044 · Cited by 28
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Exendin(9‐39) NH 2 : Recommendations for clinical use based on a systematic literature review
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“GLP-1 stimulates the release of insulin while inhibiting the release of glucagon and thus prevents the rise in postprandial blood glucose [81].”
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“In fact, based in results obtained in an animal model of GLP-1 receptor knockout, it was suggested that the pancreatic GLP-1 receptor is involved in the incretin/insulinotropic action of exendin-4 and GLP-1, and also in the hepatic portal glucose sensor action of the latter [30,31].”
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Migrenne, S., Marsollier, N., Cruciani‐Guglielmacci, C., & Magnan, C. (2006) · Current Opinion in Pharmacology · doi:10.1016/j.coph.2006.08.004 · Cited by 26
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“However, little is known about the physiological significance of this compartment.”
BackgroundGastrointestinal peptides in eating-related disorders
Smith, K., & Moran, T. H. (2021) · Physiology & Behavior · doi:10.1016/j.physbeh.2021.113456 · Cited by 25
Exenatide: a novel treatment of Type 2 diabetes
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“This insulinotropic action of GLP-1 is presumed to be a physiologic incretin action, as augmentation of insulin secretion is observed at physiologic dose levels of GLP-1 [37], the prandial increase in glucose is enhanced by a GLP-1 receptor antagonist [38], and due to the fact that the insulinotropic effect of oral gl…”
BackgroundThe incretin effect in obese adolescents with and without type 2 diabetes: impaired or intact?
Aulinger, B. A., Vahl, T. P., Prigeon, R. L., D'Alessio, D. A., & Elder, D. A. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00496.2015 · Cited by 24
Mitochondria and the Repurposing of Diabetes Drugs for Off-Label Health Benefits
Yip, J., Chiang, G. S. H., Lee, I. C. J., Lehming-Teo, R., Dai, K., Dongol, L., Wang, L. Y.-T., Teo, D. W. X., Seah, G. T., & Lehming, N. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26010364 · Cited by 30
“GLP-1 receptor agonists have not only proven to be effective in managing T2DM, obesity [103], cardiovascular risk [104], and renal dysfunction [105] but are now also emerging as a potential drug for improving health span and reducing age-related diseases [34,106,107].”
Moreno, P., Nuche‐Berenguer, B., Gutiérrez-Rojas, I., Acitores, A., Sancho, V., Valverde, I., González, N., & Villanueva‐Peñacarrillo, M. L. (2011) · Journal of Molecular Endocrinology · doi:10.1530/jme-11-0127 · Cited by 24
“…on the results obtained in a GLP-1 receptor knockout animal model, it was suggested that the pancreatic GLP-1 receptor is involved in the incretin/insulinotropic action of Ex-4 and GLP-1 and also in the hepatic portal glucose sensor action of the latter (Edwards et al. 1999, Burcelin et al. 2001).”
Equine glucagon-like peptide-1 receptor physiology
Kheder, M. H., Bailey, S. R., Dudley, K. J., Sillence, M. N., & de Laat, M. A. (2018) · PeerJ · doi:10.7717/peerj.4316 · Cited by 24
“Studies on humans and rodents have demonstrated that exendin 9-39 blocks insulin release from the pancreas, induced by both GLP-1 and exendin-4, by decreasing basal cAMP production (Chan et al., 2014; Edwards et al., 1999; Nauck et al., 2016).”
BackgroundRipken, D., van der Wielen, N., van der Meulen, J., Schuurman, T., Witkamp, R. F., Hendriks, H., & Koopmans, S. J. (2014) · Physiology & Behavior · doi:10.1016/j.physbeh.2014.11.031 · Cited by 23
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“Our current hypothesis is that the processing of proglucagon in the pancreas is not 100% specific and that a minor fraction of proglucagon actually is processed to GLP-1(7-36)-amide (in humans, amidation of GLP-1 seems to be rather extensive) (22).”
BackgroundResultInfluentialMolecular Pharmacology of the Incretin Receptors
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“Comparable studies with exendin (9–39) in humans have demonstrated the essential role of GLP-1 action for glucose control via regulation of glucagon and insulin secretion [70].”
BackgroundRetractedLocal, exendin-(9—39)-insensitive, site of action of GLP-1 in canine ileum
Daniel, E. E., Anvari, M., Fox-Threlkeld, J.-A. E. T., & McDonald, T. J. (2002) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00110.2002 · Cited by 22
“, actions to enhance pancreatic -cell growth and release insulin (22, 23, 40, 46, 50, 51, 60, 62), inhibition of gastric emptying, secretion, and intestinal motility (37, 38, 44, 59, 66, 67), central actions on the dorsal vagal nucleus and other central nervous system sites (58, 65).”
BackgroundGlucagon-like Peptide-1 Receptor Agonists for the Treatment of Type 2 Diabetes in Youth
Berman, C., Vidmar, A. P., & Chao, L. C. (2023) · touchREVIEWS in Endocrinology · doi:10.17925/ee.2023.19.1.38 · Cited by 24
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“In humans, Ex-9 can suppress the insulinotropic effects of exogenous as well as endogenous GLP-1 stimulated by an oral glucose load (Schirra et al., 1998, Edwards et al., 1999, Salehi et al., 2008).”
BackgroundInfluentialChan, S. W., Lu, Z., Lin, G., Yew, D. T. W., Yeung, C. K., & Rudd, J. A. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.03.016 · Cited by 22
“In humans, the plasma half-life of exendin (9e 39) is approximately 33 min (Edwards et al., 1999); and this relatively short duration of antiemetic action in our studies may be attributed to the rapid metabolism of exendin (9e39) in the animals and/or clearance from the brain and the ventricular…”
Forbes, S., Moonan, M., Robinson, S., Anyaoku, V., Patterson, M., Murphy, K. G., Ghatei, M. A., Bloom, S. R., & Johnston, D. G. (2004) · Clinical Endocrinology · doi:10.1111/j.1365-2265.2004.02172.x · Cited by 21
Self-citationEffects of incretin-based therapies on renal function
Tsimihodimos, V., & Elisaf, M. (2017) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2017.10.049 · Cited by 21
“They participate in the regulation of carbohydrate homeostasis through the increase in the production of insulin in a glucose-dependent manner and the suppression of the production of glucagon by the pancreatic alpha cells (Edwards et al., 1999; Meier et al., 2004).”
BackgroundShah, M., LAURENTI, M. C., Man, C. D., Ma, J., Cobelli, C., Rizza, R. A., & Vella, A. V. (2018) · Metabolism · doi:10.1016/j.metabol.2018.12.005 · Cited by 20
“Based on prior experiments [31-33] and the estimated portal concentrations of GLP-1 [34], this rate should result in near complete inhibition of GLP-1 actions at its cognate receptor [35].”
BackgroundThe GLP‐1 system as a therapeutic target
Edwards, M. C. B. (2005) · Annals of Medicine · doi:10.1080/07853890510037400 · Cited by 19
“Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon-like peptide-1(7-36)amide, peptide histidine methionine and is responsible for their degradation in human serum.”
BackgroundInfluentialLi, J., Rawson, J., Chea, J., Tang, W., MIAO, L. N., Sui, F., Li, C., Poku, E. K., Shively, J. E., & KANDEEL, F. R. (2019) · Scientific Reports · doi:10.1038/s41598-019-42172-3 · Cited by 19
Vasto, S., Gaudio, F. D., Raso, M., Sabatino, L., Caldarella, R., PASQUALE, C. D., Rosa, L. D., & Baldassano, S. (2022) · Nutrients · doi:10.3390/nu14071351 · Cited by 18
“However, there is an important difference between GLP-1 and GIP, because GLP-1 inhibits glucagon secretion [41] while GIP seems influencing, in quantitative way, insulin signaling [39].”
BackgroundRapid hepatic metabolism blunts the endocrine action of portally infused GLP-1 in male rats
Aulinger, B. A., Perabò, M., Seeley, R. J., Parhofer, K. G., & D’Alessio, D. A. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00298.2019 · Cited by 20
“On the other hand, the amount of insulin stimulated through the portal neural pathway was small and did not affect glucose clearance and is at odds with the notion that GLP-1 is the major mediator of to the incretin effect and postprandial glucose clearance in rodents (22, 33) and humans (14, 32).”
BackgroundOsaka, T., Hamaguchi, M., & Fukui, M. (2023) · Clinical Medicine Insights Endocrinology and Diabetes · doi:10.1177/11795514231161885 · Cited by 20
Drab, S. R. (2009) · Pharmacotherapy The Journal of Human Pharmacology and Drug Therapy · doi:10.1592/phco.29.pt2.43s · Cited by 18
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“The glucagon-like peptide 1 (GLP-1) is secreted by L cells of the terminal ileum and colon after food intake under physiological conditions [3] and its half-life is only of 1–2 minutes [4].”
BackgroundParker, J. C., Lavery, K. S., Irwin, N., Green, B., Greer, B., Harriott, P., O'Harte, F. P. M., Gault, V. A., & Flatt, P. R. (2006) · Journal of Endocrinology · doi:10.1677/joe.1.06904 · Cited by 18
“Thus, the antagonist actions of GLP-1(9–36) amide appear minor compared with exendin(9–39)amide (Kolligs et al. 1995, Edwards et al. 1999).”
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Abbara, A., Narayanaswamy, S., Izzi‐Engbeaya, C. N., Comninos, A. N., Clarke, S. A., Malik, Z. A., Papadopoulou, D., Clobentz, A., Sarang, Z., Bassett, P., et al. (2018) · Neuroendocrinology · doi:10.1159/000488452 · Cited by 17
Glucolipotoxicity and GLP-1 secretion
Hong, J.-H., Kim, D., & Lee, M. (2021) · BMJ Open Diabetes Research & Care · doi:10.1136/bmjdrc-2020-001905 · Cited by 17
Xie, Z., Yang, Z., Tian, D., & Chen, Y. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1618079 · Cited by 21
The incretin system and cardiometabolic disease
Szmitko, P. E., Leiter, L. A., & Verma, S. (2010) · Canadian Journal of Cardiology · doi:10.1016/s0828-282x(10)70010-6 · Cited by 17
“glucose-stimulated insulin levels (44,45).”
A sandwich ELISA for measurement of the primary glucagon-like peptide-1 metabolite
Albrechtsen, N. J. W., Asmar, A., Jensen, F. H., Toräng, S., Simonsen, L., Kuhre, R. E., Asmar, M., Veedfald, S., Plamboeck, A., Knop, F. K., et al. (2017) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00005.2017 · Cited by 15
“This accounts for a significant part of the total postprandial insulin response in healthy humans (20) as demonstrated in experiments using the GLP-1 receptor (GLP-1R) antagonist, exendin 9–39 (9, 27).”
Larsen, M. O., Rolin, B., Ribel, U., Wilken, M., Deacon, C. F., Svendsen, O., Gotfredsen, C. F., & Carr, R. D. (2003) · Journal of Diabetes Research · doi:10.1155/edr.2003.93 · Cited by 17
“Receptor antagonists have been used to demonstrate the physiological role of both incretin hormones in the maintenance of normal glucose homeostasis [13, 38, 59, 66]; mice with targeted deletions of either the GLP-1 or the GIP receptor become glucose intolerant [43, 60], confirming the importance of both peptides in t…”
MethodMedicinal Chemistry of Glucagon-Like Peptide Receptor Agonists
Jones, L. H., & Price, D. A. (2013) · Progress in medicinal chemistry · doi:10.1016/b978-0-444-62652-3.00002-8 · Cited by 15
Roges, O. A., Baron, M., & Philis‐Tsimikas, A. (2005) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.14.6.705 · Cited by 15
“The physiological importance of GIP and GLP-1 in glucose metabolism has been demonstrated using GIP and GLP-1 receptor antagonists [33-36] as well as receptor-knockout animal models [37-39].”
BackgroundGabe, M. B. N., Gasbjerg, L. S., Gadgaard, S., Lindquist, P., Holst, J. J., & ROSENKILDE, M. M. (2022) · British Journal of Pharmacology · doi:10.1111/bph.15866 · Cited by 14
Central Control of Glucose Homeostasis
Puglianiello, A., & Cianfarani, S. (2006) · The Review of Diabetic Studies · doi:10.1900/rds.2006.3.54 · Cited by 14
“Blockade or reduction of GLP-1 determined abnormally high glucose levels following glucose administration [51, 52].”
BackgroundA liquid chromatography-mass spectrometry assay for quantification of Exendin[9-39] in human plasma
Lasaosa, M., Patel, P., Givler, S., et al. (2013) · Journal of Chromatography B · doi:10.1016/j.jchromb.2013.12.010 · Cited by 13
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“GLP-1 has an important role in regulating postprandial blood glucose levels because it stimulates insulin secretion in a glucose-dependent manner and inhibits glucagon secretion.(2) Despite its unique nature and desirable effects, such as the enhancement of pancreatic β-cell mass, inhibition of gastric emptying, and r…”
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Glucagon‐like peptide‐1‐based therapies: new developments and emerging data
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Integration of Glucagon-Like Peptide 1 Receptor Actions Through the Central Amygdala
Duran, M., Willis, J. R., Dalvi, N., Fokakis, Z. N., VIRKUS, S., & Hardaway, J. A. (2025) · Endocrinology · doi:10.1210/endocr/bqaf019 · Cited by 12
Exendin-4 Inhibits HMGB1-Induced Inflammatory Responses in HUVECs and in Murine Polymicrobial Sepsis
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“Exendin 9-39 (EX9), a fragment of EX4 composed of 37 amino acids, is a GLP-1 receptor antagonist, which inhibits GLP-1-induced cAMP production and blocks GLP-1-induced insulin secretion [14].”
Glucagon-like peptide-1 improves insulin and proinsulin binding on RINm5F cells and human monocytes
Ebinger, M., Jehle, D. R., Fussgaenger, R. D., Fehmann, H. C., & Jehle, P. M. (2000) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.2000.279.1.e88 · Cited by 13
“RINm5F cells were incubated for 2 h with 1 nM of GLP-1 alone or in combination with the GLP-1 receptor agonist exendin-4 or the GLP-1 receptor antagonist exendin-(9O39) amide (8, 17).”
MethodThe Gut: A Key to the Pathogenesis of Type 2 Diabetes?
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Self-citationOrdered Eating and Its Effects on Various Postprandial Health Markers: A Systematic Review
Ferguson, B. K., & Wilson, P. B. (2022) · Journal of the American Nutrition Association · doi:10.1080/27697061.2022.2161664 · Cited by 11
DPIV — Natural Substrates of Medical Importance
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Sir David Cuthbertson Medal Lecture Bariatric surgery as a model to study appetite control
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“It also suppresses gastric acid secretion and delays gastric emptying((53,54)).”
BackgroundEndogenously released GLP-1 is not sufficient to alter postprandial glucose regulation in the dog
Johnson, K., Farmer, T. E., Schurr, K., Donahue, E. P., Farmer, B., Neal, D. W., & Cherrington, A. D. (2011) · Endocrine · doi:10.1007/s12020-011-9441-x · Cited by 9
“This rate of Ex-9 infusion has been shown to completely inhibit GLP-1R activation in humans [ 10 ].”
InfluentialWilson, J. R., Brown, N. J., Nian, H., Yu, C., Bidlingmaier, M., & Devin, J. K. (2018) · Journal of the American Heart Association · doi:10.1161/jaha.117.008000 · Cited by 8
“Ban et al(41) demonstrated that GLP-1 (9-36) increases endothelium-dependent vasodilation in mice lacking a GLP-1 receptor.”
BackgroundAndersen, O., Haugaard, S. B., Holst, J. J., Deacon, C. F., Iversen, J., Andersen, U. B., Nielsen, J., & Madsbad, S. (2005) · HIV Medicine · doi:10.1111/j.1468-1293.2005.00270.x · Cited by 8
Repurposing metabolic drugs as anti-inflammatory agents
Hogan, A. E., Davis, C., Jenkins, B., Jones, N., & O'Shea, D. B. (2025) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2025.07.003 · Cited by 14
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“Frontiers in Endocrinology 10 after a meal (64, 65).”
BackgroundTreatment of Type 2 diabetes mellitus based on glucagon-like peptide-1
Holst, J. J. (1999) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.8.9.1409 · Cited by 6
Lu, Z., Ngan, M. P., Lin, G., Yew, D. T. W., Fan, X., Andrews, P. L. R., & Rudd, J. A. (2017) · Oncotarget · doi:10.18632/oncotarget.21859 · Cited by 7
“infusion of exendin (9-39) in healthy human subjects had no effect on BP [59].”
BackgroundSalehi, M., Gastaldelli, A., & D’Alessio, D. A. (2019) · Diabetes Obesity and Metabolism · doi:10.1111/dom.13676 · Cited by 7
Utilizing the GLP-1 signaling system to treat diabetes: Sorting through the pharmacologic approaches
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Assessment of the incretin effect in healthy subjects: concordance between clamp and OGTT methods
Aulinger, B. A., & D’Alessio, D. A. (2023) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00104.2022 · Cited by 6
GLP-1/GLP-1RAs: New Options for the Drug Treatment of NAFLD
Jiang, H., & Zang, L. (2024) · Current Pharmaceutical Design · doi:10.2174/0113816128283153231226103218 · Cited by 6
Exendin-4 inhibits endothelial protein C receptor shedding in vitro and in vivo
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Zukünftige Angriffspunkte für die Therapie des Typ-2-Diabetes
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Elucidating the glucose‐lowering effect of the bile acid sequestrant sevelamer
Nerild, H. H., Brønden, A., Haddouchi, A. E., Ellegaard, A., Hartmann, B., Rehfeld, J. F., Holst, J. J., Sonne, D. P., Vilsbøll, T., & Knop, F. K. (2023) · Diabetes Obesity and Metabolism · doi:10.1111/dom.15421 · Cited by 5
Hædersdal, S., Lund, A., Nielsen-Hannerup, E., Maagensen, H., Forman, J. L., Holst, J. J., Knop, F. K., & Vilsbøll, T. (2022) · European Journal of Endocrinology · doi:10.1530/eje-22-0291 · Cited by 6
Sreenan, S., Mittal, A. A., Dralyuk, F., Pugh, W. L., Polonsky, K. S., & Roe, M. W. (2000) · Metabolism · doi:10.1053/meta.2000.18555 · Cited by 5
Nauck, M. A., Schmidt, W. E., & Meier, J. J. (2007) · Springer eBooks · doi:10.1007/978-0-387-69737-6_12 · Cited by 5
Rachman, J. (2004) · Diabetic Medicine · doi:10.1111/j.1466-5468.2004.1180h.x · Cited by 6
Mulherin, A. J., Oh, A., Kim, H., Grieco, A., Lauffer, L., & Brubaker, P. (2011) · Obesity and metabolism · doi:10.14341/2071-8713-5305 · Cited by 4
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Metadata
- Authors
- Edwards, C. M., Todd, J. F., Mahmoudi, M., Wang, Z., Wang, R. M., Ghatei, M. A., & Bloom, S. R.
- Affiliations
- Hammersmith Hospital (GB)
- Venue
- Diabetes
- Publisher
- American Diabetes Association
- Published
- 1999-01-01
- Volume
- 48
- Issue
- 1
- Pages
- 86-93
- ISSN
- 0012-1797 (ISSN-L)
- 1939-327X
- OpenAlex
- W2146581079
- Cited by
- 344
- References
- 0
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 7 · 2023: 10 · 2022: 7 · 2021: 8 · 2020: 9 · 2019: 17 · 2018: 12 · 2017: 12 · 2016: 16 · 2015: 16 · 2014: 13 · 2013: 19 · 2012: 8
- FWCI
- 9.68
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Diabetes (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Treatment and Management
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Pancreatic function and diabetes
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Diabetes Management and Research
- Keywords
- glucagon-like peptide-1, exendin-9-39, incretins, postprandial blood glucose, glucose-stimulated insulin secretion, pancreatic islets, glucagon suppression, gastric emptying, glucose tolerance, insulinotropic effect
- MeSH terms
- Insulin Secretion, Eating, Glucagon, Glucose, Glucose Tolerance Test, Humans, Insulin, Islets of Langerhans, Peptide Fragments, Protein Precursors, Cytokines, Glucagon-Like Peptide 1, In Vitro Techniques
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